CML1_MOUSE
ID CML1_MOUSE Reviewed; 371 AA.
AC P97468;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Chemerin-like receptor 1;
DE AltName: Full=Chemokine-like receptor 1;
DE AltName: Full=G-protein coupled receptor DEZ;
GN Name=Cmklr1; Synonyms=Dez, Gpcr27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9144535; DOI=10.1006/bbrc.1997.6455;
RA Methner A., Hermey G., Schinke B., Hermans-Borgmeyer I.;
RT "A novel G protein-coupled receptor with homology to neuropeptide and
RT chemoattractant receptors expressed during bone development.";
RL Biochem. Biophys. Res. Commun. 233:336-342(1997).
RN [2]
RP LIGAND-BINDING, AND FUNCTION.
RX PubMed=15753205; DOI=10.1084/jem.20042031;
RA Arita M., Bianchini F., Aliberti J., Sher A., Chiang N., Hong S., Yang R.,
RA Petasis N.A., Serhan C.N.;
RT "Stereochemical assignment, antiinflammatory properties, and receptor for
RT the omega-3 lipid mediator resolvin E1.";
RL J. Exp. Med. 201:713-722(2005).
RN [3]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16863918; DOI=10.1016/j.exphem.2006.03.011;
RA Zabel B.A., Ohyama T., Zuniga L., Kim J.Y., Johnston B., Allen S.J.,
RA Guido D.G., Handel T.M., Butcher E.C.;
RT "Chemokine-like receptor 1 expression by macrophages in vivo: regulation by
RT TGF-beta and TLR ligands.";
RL Exp. Hematol. 34:1106-1114(2006).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17767914; DOI=10.1016/j.bbrc.2007.08.104;
RA Roh S.G., Song S.H., Choi K.C., Katoh K., Wittamer V., Parmentier M.,
RA Sasaki S.;
RT "Chemerin--a new adipokine that modulates adipogenesis via its own
RT receptor.";
RL Biochem. Biophys. Res. Commun. 362:1013-1018(2007).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17635925; DOI=10.1074/jbc.m700793200;
RA Goralski K.B., McCarthy T.C., Hanniman E.A., Zabel B.A., Butcher E.C.,
RA Parlee S.D., Muruganandan S., Sinal C.J.;
RT "Chemerin, a novel adipokine that regulates adipogenesis and adipocyte
RT metabolism.";
RL J. Biol. Chem. 282:28175-28188(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18242188; DOI=10.1016/j.febslet.2008.01.023;
RA Takahashi M., Takahashi Y., Takahashi K., Zolotaryov F.N., Hong K.S.,
RA Kitazawa R., Iida K., Okimura Y., Kaji H., Kitazawa S., Kasuga M.,
RA Chihara K.;
RT "Chemerin enhances insulin signaling and potentiates insulin-stimulated
RT glucose uptake in 3T3-L1 adipocytes.";
RL FEBS Lett. 582:573-578(2008).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=19841182; DOI=10.4049/jimmunol.0901037;
RA Luangsay S., Wittamer V., Bondue B., De Henau O., Rouger L., Brait M.,
RA Franssen J.D., de Nadai P., Huaux F., Parmentier M.;
RT "Mouse ChemR23 is expressed in dendritic cell subsets and macrophages, and
RT mediates an anti-inflammatory activity of chemerin in a lung disease
RT model.";
RL J. Immunol. 183:6489-6499(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; THR-340; SER-347;
RP SER-350 AND THR-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for the chemoattractant adipokine chemerin/RARRES2
CC and for the omega-3 fatty acid derived molecule resolvin E1.
CC Interaction with RARRES2 initiates activation of G proteins G(i)/G(o)
CC and beta-arrestin pathways inducing cellular responses via second
CC messenger pathways such as intracellular calcium mobilization,
CC phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3,
CC MAPK14/P38MAPK and PI3K leading to multifunctional effects, like,
CC reduction of immune responses, enhancing of adipogenesis and
CC angionesis. Resolvin E1 down-regulates cytokine production in
CC macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-
CC kappa-B (By similarity). Positively regulates adipogenesis and
CC adipocyte metabolism. {ECO:0000250, ECO:0000269|PubMed:15753205,
CC ECO:0000269|PubMed:16863918, ECO:0000269|PubMed:17635925}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16863918};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the differentiated adipocytes (at
CC protein level). Ubiquitous. Highly expressed in adipose tissue and
CC immature plasmacytoid dendritic cells (DCs) and at lower levels in
CC myeloid DCs, macrophages, and NK cells. Expressed on macrophages
CC isolated from different tissues, including peritoneal cavities, pleural
CC cavities and spleen. {ECO:0000269|PubMed:16863918,
CC ECO:0000269|PubMed:17635925, ECO:0000269|PubMed:17767914,
CC ECO:0000269|PubMed:18242188, ECO:0000269|PubMed:19841182}.
CC -!- DEVELOPMENTAL STAGE: Expressed during bone development and in adult
CC parathyroid glands. Expressed at 11 dpc in the caudal part of the
CC tongue and the umbilical cord and the expression in the tongue was
CC maintained throughout adulthood. Expression increases in bone and
CC cartilaginous forming zones of embryo up to stage 14.5 dpc and at 16.5
CC dpc expression is seen in the lung. {ECO:0000269|PubMed:9144535}.
CC -!- INDUCTION: Down-regulated by bacterial lipopolysaccharide (LPS), IFN-
CC alpha and TNF on macrophages. {ECO:0000269|PubMed:16863918}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; U79525; AAB53789.1; -; mRNA.
DR CCDS; CCDS19551.1; -.
DR PIR; JC5498; JC5498.
DR RefSeq; NP_032179.1; NM_008153.3.
DR RefSeq; XP_006530227.1; XM_006530164.3.
DR RefSeq; XP_006530228.1; XM_006530165.2.
DR RefSeq; XP_006530229.1; XM_006530166.2.
DR AlphaFoldDB; P97468; -.
DR SMR; P97468; -.
DR STRING; 10090.ENSMUSP00000036316; -.
DR BindingDB; P97468; -.
DR ChEMBL; CHEMBL4523269; -.
DR GlyGen; P97468; 2 sites.
DR iPTMnet; P97468; -.
DR PhosphoSitePlus; P97468; -.
DR jPOST; P97468; -.
DR PaxDb; P97468; -.
DR PRIDE; P97468; -.
DR ProteomicsDB; 283637; -.
DR Antibodypedia; 9299; 583 antibodies from 36 providers.
DR DNASU; 14747; -.
DR Ensembl; ENSMUST00000047936; ENSMUSP00000036316; ENSMUSG00000042190.
DR GeneID; 14747; -.
DR KEGG; mmu:14747; -.
DR UCSC; uc012ebo.1; mouse.
DR CTD; 1240; -.
DR MGI; MGI:109603; Cmklr1.
DR VEuPathDB; HostDB:ENSMUSG00000042190; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P97468; -.
DR OMA; TACVVIW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; P97468; -.
DR TreeFam; TF330976; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR BioGRID-ORCS; 14747; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cmklr1; mouse.
DR PRO; PR:P97468; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97468; protein.
DR Bgee; ENSMUSG00000042190; Expressed in epididymal fat pad and 141 other tissues.
DR ExpressionAtlas; P97468; baseline and differential.
DR Genevisible; P97468; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0097004; F:adipokinetic hormone binding; ISS:UniProtKB.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; ISO:MGI.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
DR InterPro; IPR002258; CML1.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF49; PTHR24225:SF49; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01126; DEZORPHANR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..371
FT /note="Chemerin-like receptor 1"
FT /id="PRO_0000069308"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..318
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35786"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 371 AA; 41815 MW; CDBE19305244C0B3 CRC64;
MEYDAYNDSG IYDDEYSDGF GYFVDLEEAS PWEAKVAPVF LVVIYSLVCF LGLLGNGLVI
VIATFKMKKT VNTVWFVNLA VADFLFNIFL PMHITYAAMD YHWVFGKAMC KISNFLLSHN
MYTSVFLLTV ISFDRCISVL LPVWSQNHRS IRLAYMTCSA VWVLAFFLSS PSLVFRDTAN
IHGKITCFNN FSLAAPESSP HPAHSQVVST GYSRHVAVTV TRFLCGFLIP VFIITACYLT
IVFKLQRNRL AKNKKPFKII ITIIITFFLC WCPYHTLYLL ELHHTAVPSS VFSLGLPLAT
AVAIANSCMN PILYVFMGHD FRKFKVALFS RLANALSEDT GPSSYPSHRS FTKMSSLNEK
ASVNEKETST L
